Cysteine residues in proteins are of great interest to Proteomics researchers. These amino acids are reactive and form from di-sulfide bonds breaking apart. When a technician reduces these bonds with a reagent like Dithiothreitol (DTT), free Sulfhydryl groups become present and these can react with a variety of functional groups. Often, a digestion protocol will call for reduction of the di-sulfides and consequent akylation with a reagent such as Iodoactemide (or Iodoacetic Acid) to cap the -SH groups.
>>Read the entire tutorial at IonSource.com
IonSource is a great resource for more information on this procedure We invite you to visit the site and learn more about S-Carboxymethylation of the Amino Acid Residue Cysteine with the Alkylating Agent Iodoacetic Acid.
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